IDH3G_HUMAN
ID IDH3G_HUMAN Reviewed; 393 AA.
AC P51553; E9PDD5; Q9BUU5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial;
DE AltName: Full=Isocitric dehydrogenase subunit gamma;
DE AltName: Full=NAD(+)-specific ICDH subunit gamma;
DE Flags: Precursor;
GN Name=IDH3G;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9286695; DOI=10.1006/geno.1997.4822;
RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.;
RT "Genomic organization of two novel genes on human Xq28: compact head to
RT head arrangement of IDH gamma and TRAP delta is conserved in rat and
RT mouse.";
RL Genomics 44:8-14(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=10601238; DOI=10.1074/jbc.274.52.36866;
RA Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S.,
RA Lee I.J., Song B.J., Huh T.-L.;
RT "Identification and functional characterization of a novel, tissue-specific
RT NAD+-dependent isocitrate dehydrogenase beta subunit isoform.";
RL J. Biol. Chem. 274:36866-36875(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11256614; DOI=10.1093/embo-reports/kvd058;
RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.;
RT "Systematic subcellular localization of novel proteins identified by large-
RT scale cDNA sequencing.";
RL EMBO Rep. 1:287-292(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, COFACTOR, AND MUTAGENESIS OF
RP LYS-190.
RX PubMed=28139779; DOI=10.1038/srep41882;
RA Ma T., Peng Y., Huang W., Liu Y., Ding J.;
RT "The beta and gamma subunits play distinct functional roles in the
RT alpha2betagamma heterotetramer of human NAD-dependent isocitrate
RT dehydrogenase.";
RL Sci. Rep. 7:41882-41882(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 40-393 IN COMPLEX WITH MAGNESIUM
RP AND CITRATE, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 40-393 OF MUTANT
RP ALA-190 IN COMPLEX WITH MAGNESIUM; ADP AND CITRATE, SUBUNIT, COFACTOR,
RP ACTIVITY REGULATION, ALLOSTERIC ACTIVATION, AND MUTAGENESIS OF ASN-117;
RP THR-120; SER-130; ASN-133; ARG-136; ARG-167; GLU-173; TYR-174; LYS-190;
RP ASP-229; TYR-276; ARG-311; ASN-312; THR-313; LYS-315 AND ASN-324.
RX PubMed=28098230; DOI=10.1038/srep40921;
RA Ma T., Peng Y., Huang W., Ding J.;
RT "Molecular mechanism of the allosteric regulation of the alphagamma
RT heterodimer of human NAD-dependent isocitrate dehydrogenase.";
RL Sci. Rep. 7:40921-40921(2017).
CC -!- FUNCTION: Regulatory subunit which plays a role in the allosteric
CC regulation of the enzyme catalyzing the decarboxylation of isocitrate
CC (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha
CC (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the
CC alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal
CC activity but the full activity of the heterotetramer (containing two
CC subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly
CC and cooperative function of both heterodimers.
CC {ECO:0000269|PubMed:28139779}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28139779};
CC Note=Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in
CC presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per
CC subunit. {ECO:0000269|PubMed:28139779};
CC -!- ACTIVITY REGULATION: The heterotetramer and the heterodimer composed of
CC IDH3A and IDH3G subunits can be allosterically activated by citrate
CC (CIT) or/and ADP, and the two activators can act independently or
CC synergistically. The heterodimer composed of IDH3A and IDH3B subunits
CC cannot be allosterically regulated and the allosteric regulation of the
CC heterotetramer is through the IDH3G subunit and not the IDH3B subunit.
CC The IDH3G subunit contains the allosteric site which consists of a CIT-
CC binding site and an ADP-binding site, and the binding of CIT and ADP
CC causes conformational changes at the allosteric site which are
CC transmitted to the active site in the catalytic subunit (IDH3A) through
CC a cascade of conformational changes at the heterodimer interface,
CC leading to stabilization of the isocitrate-binding at the active site
CC and thus activation of the enzyme. ATP can activate the heterotetramer
CC and the heterodimer composed of IDH3A and IDH3G subunits at low
CC concentrations but inhibits their activities at high concentrations,
CC whereas ATP exhibits only inhibitory effect on the heterodimer composed
CC of IDH3A and IDH3B subunits. {ECO:0000269|PubMed:28098230,
CC ECO:0000269|PubMed:28139779}.
CC -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC containing one IDH3A and one IDH3B subunit and the heterodimer
CC containing one IDH3A and one IDH3G subunit assemble into a
CC heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC one of IDH3G) and further into the heterooctamer.
CC {ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779}.
CC -!- INTERACTION:
CC P51553; P50213: IDH3A; NbExp=5; IntAct=EBI-1210876, EBI-355999;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11256614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51553-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51553-2; Sequence=VSP_046771;
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; Z68907; CAA93143.1; -; mRNA.
DR EMBL; Z68129; CAA92214.1; -; Genomic_DNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U40272; AAD09357.1; -; mRNA.
DR EMBL; BC000933; AAH00933.1; -; mRNA.
DR EMBL; BC001902; AAH01902.1; -; mRNA.
DR CCDS; CCDS14730.1; -. [P51553-1]
DR CCDS; CCDS44019.1; -. [P51553-2]
DR RefSeq; NP_004126.1; NM_004135.3. [P51553-1]
DR RefSeq; NP_777358.1; NM_174869.2. [P51553-2]
DR PDB; 5GRE; X-ray; 2.65 A; B=40-393.
DR PDB; 5GRF; X-ray; 2.50 A; B=40-393.
DR PDB; 5GRH; X-ray; 2.80 A; B=40-393.
DR PDB; 5GRI; X-ray; 2.31 A; B=40-393.
DR PDB; 5GRL; X-ray; 2.79 A; B=40-393.
DR PDB; 5YVT; X-ray; 2.40 A; B=40-393.
DR PDB; 6L57; X-ray; 2.30 A; B=40-393.
DR PDB; 6L59; X-ray; 2.25 A; B=40-393.
DR PDB; 7CE3; X-ray; 3.47 A; B=40-393.
DR PDBsum; 5GRE; -.
DR PDBsum; 5GRF; -.
DR PDBsum; 5GRH; -.
DR PDBsum; 5GRI; -.
DR PDBsum; 5GRL; -.
DR PDBsum; 5YVT; -.
DR PDBsum; 6L57; -.
DR PDBsum; 6L59; -.
DR PDBsum; 7CE3; -.
DR AlphaFoldDB; P51553; -.
DR SMR; P51553; -.
DR BioGRID; 109647; 57.
DR ComplexPortal; CPX-553; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR CORUM; P51553; -.
DR IntAct; P51553; 10.
DR MINT; P51553; -.
DR STRING; 9606.ENSP00000217901; -.
DR DrugBank; DB06757; Manganese.
DR DrugBank; DB00157; NADH.
DR iPTMnet; P51553; -.
DR PhosphoSitePlus; P51553; -.
DR BioMuta; IDH3G; -.
DR DMDM; 1708404; -.
DR EPD; P51553; -.
DR jPOST; P51553; -.
DR MassIVE; P51553; -.
DR MaxQB; P51553; -.
DR PaxDb; P51553; -.
DR PeptideAtlas; P51553; -.
DR PRIDE; P51553; -.
DR ProteomicsDB; 19639; -.
DR ProteomicsDB; 56332; -. [P51553-1]
DR Antibodypedia; 408; 266 antibodies from 32 providers.
DR DNASU; 3421; -.
DR Ensembl; ENST00000217901.10; ENSP00000217901.5; ENSG00000067829.20. [P51553-1]
DR Ensembl; ENST00000370092.7; ENSP00000359110.3; ENSG00000067829.20. [P51553-2]
DR GeneID; 3421; -.
DR KEGG; hsa:3421; -.
DR MANE-Select; ENST00000217901.10; ENSP00000217901.5; NM_004135.4; NP_004126.1.
DR UCSC; uc004fip.4; human. [P51553-1]
DR CTD; 3421; -.
DR GeneCards; IDH3G; -.
DR HGNC; HGNC:5386; IDH3G.
DR HPA; ENSG00000067829; Low tissue specificity.
DR MIM; 300089; gene.
DR neXtProt; NX_P51553; -.
DR OpenTargets; ENSG00000067829; -.
DR PharmGKB; PA29634; -.
DR VEuPathDB; HostDB:ENSG00000067829; -.
DR eggNOG; KOG0784; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR InParanoid; P51553; -.
DR OMA; GTSMFEP; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; P51553; -.
DR TreeFam; TF315033; -.
DR BioCyc; MetaCyc:ENSG00000067829-MON; -.
DR BRENDA; 1.1.1.41; 2681.
DR PathwayCommons; P51553; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; P51553; -.
DR SignaLink; P51553; -.
DR SIGNOR; P51553; -.
DR BioGRID-ORCS; 3421; 7 hits in 712 CRISPR screens.
DR ChiTaRS; IDH3G; human.
DR GeneWiki; IDH3G; -.
DR GenomeRNAi; 3421; -.
DR Pharos; P51553; Tbio.
DR PRO; PR:P51553; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51553; protein.
DR Bgee; ENSG00000067829; Expressed in right hemisphere of cerebellum and 208 other tissues.
DR ExpressionAtlas; P51553; baseline and differential.
DR Genevisible; P51553; HS.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Magnesium; Manganese;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..393
FT /note="Isocitrate dehydrogenase [NAD] subunit gamma,
FT mitochondrial"
FT /id="PRO_0000014449"
FT BINDING 120
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 133
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared with catalytic subunit"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 312
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 313
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:28098230"
FT BINDING 324
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:28098230"
FT VAR_SEQ 361..393
FT /note="MHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA -> VRFPSHPTLLPRPVS
FT PCSLL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046771"
FT MUTAGEN 117
FT /note="N->A: No effect on the activation of the heterodimer
FT composed of IDH3A and IDH3G subunits by citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 120
FT /note="T->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 130
FT /note="S->A: No significant effect on the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 133
FT /note="N->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 136
FT /note="R->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 167
FT /note="R->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 173
FT /note="E->A: No effect on the activation of the heterodimer
FT composed of IDH3A and IDH3G subunits by citrate and ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 174
FT /note="Y->F: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 190
FT /note="K->A: Complete loss of the activation of the
FT heterotetramer and the heterodimer composed of IDH3A and
FT IDH3G subunits by citrate and ADP."
FT /evidence="ECO:0000269|PubMed:28098230,
FT ECO:0000269|PubMed:28139779"
FT MUTAGEN 229
FT /note="D->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by citrate
FT and ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 276
FT /note="Y->F: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by citrate
FT and ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 311
FT /note="R->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by
FT citrate."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 312
FT /note="N->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 313
FT /note="T->A: Significantly impairs the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 315
FT /note="K->A: No significant effect on the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT MUTAGEN 324
FT /note="N->A: Complete loss of the activation of the
FT heterodimer composed of IDH3A and IDH3G subunits by ADP."
FT /evidence="ECO:0000269|PubMed:28098230"
FT CONFLICT 267
FT /note="F -> L (in Ref. 4; AAH01902)"
FT /evidence="ECO:0000305"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5GRH"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:6L59"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:6L59"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6L59"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:6L57"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6L59"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:6L59"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7CE3"
SQ SEQUENCE 393 AA; 42794 MW; A0870F2B7D228A37 CRC64;
MALKVATVAG SAAKAVLGPA LLCRPWEVLG AHEVPSRNIF SEQTIPPSAK YGGRHTVTMI
PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET
NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE
SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA
ARYPQITFEN MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG
HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN
MHTPDIGGQG TTSEAIQDVI RHIRVINGRA VEA
